Results 291 to 300 of about 336,318 (323)

Exploratory Covalent Docking of Michael-Acceptor Natural Products at Reactive Cysteines in Cancer Tyrosine Kinases. [PDF]

open access: yesInt J Mol Sci
Lobo F   +5 more
europepmc   +1 more source
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Protein tyrosine kinases and cancer

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 1997
4. Tyrosine kinase activation by mutation . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . F222 4.1. BCR–ABL and human leukemia . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . F222 4.2. TEL–ABL and human leukemia . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . F224 4.3.
K S, Kolibaba, B J, Druker
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Protein Tyrosine Kinase Activity Assays

Current Protocols in Pharmacology, 1999
AbstractProtein tyrosine kinases (PTKs) are ubiquitous enzymes that are integrally involved in the regulation of transformation mechanisms, normal and pathological growth, cell cycle regulation, immune responses, and a variety of intracellular signaling mechanisms.
B E, Hawes, T, van Biesen
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Nuclear protein tyrosine kinases

Trends in Biochemical Sciences, 1994
Protein tyrosine phosphorylation plays an important role in the transduction of extracellular signals. The prototypical protein tyrosine kinases are localized at the plasma membrane and are coupled to receptors that bind extracellular factors. Thus, protein tyrosine phosphorylation was previously thought to occur only in the cytoplasm. However, several
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Inhibitors of protein tyrosine kinases

Current Opinion in Biotechnology, 1995
The description in the past year of several novel protein tyrosine kinase inhibitors, which exhibit dramatic improvements in potency and specificity over earlier agents, will be considered a major turning point in the field. These compounds appear to have the necessary pharmacological properties to finally allow clarification of whether suppression of ...
D W, Fry, A J, Bridges
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Protein tyrosine kinase–substrate interactions

Current Opinion in Structural Biology, 2006
Protein tyrosine kinases (PTKs) are enzymes that catalyze the phosphorylation of tyrosyl residues. They are important in physiological and pathophysiological processes. Protein substrates of PTKs are often difficult to discern, but recently reported methods have helped to identify targets and characterize their structural interactions with kinases.
Ron, Bose   +3 more
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Non-receptor protein tyrosine kinases

Frontiers in Bioscience, 2003
The protein tyrosine kinases (PTKs) are enzymes catalyzing the transfer of the gamma-phosphate group of ATP to the hydroxyl groups of specific tyrosine residues in peptides. Although phosphotransfer reactions catalyzed by various PTKs are similar with regard to their basic mechanisms, their biological functions demonstrate a considerable degree of ...
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src-related protein tyrosine kinases

1989
Tyrosine protein kinases (TPKs) catalyze the transfer of phosphate groups from nucleotide triphosphates to tyrosine residues on proteins and peptides. While phosphorylation of proteins on tyrosine residues is a well-known post-radiational event detected in different regulatory systems, only a small number of cellular proteins are known substrates for ...
A, Veillette, J B, Bolen
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